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Database: UniProt
Entry: A0A6P8EVQ1_CLUHA
LinkDB: A0A6P8EVQ1_CLUHA
Original site: A0A6P8EVQ1_CLUHA 
ID   A0A6P8EVQ1_CLUHA        Unreviewed;      1393 AA.
AC   A0A6P8EVQ1;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   28-JAN-2026, entry version 23.
DE   SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X6 {ECO:0000313|RefSeq:XP_031414977.1};
GN   Name=LOC105894554 {ECO:0000313|RefSeq:XP_031414977.1};
OS   Clupea harengus (Atlantic herring).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Clupei; Clupeiformes; Clupeoidei;
OC   Clupeidae; Clupea.
OX   NCBI_TaxID=7950 {ECO:0000313|Proteomes:UP000515152, ECO:0000313|RefSeq:XP_031414977.1};
RN   [1] {ECO:0000313|RefSeq:XP_031414977.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
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DR   RefSeq; XP_031414977.1; XM_031559117.1.
DR   GeneID; 105894554; -.
DR   Proteomes; UP000515152; Chromosome 21.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR   CDD; cd00247; Endostatin-like; 1.
DR   FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR   FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.40.1620.70; -; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR050149; Collagen_superfamily.
DR   InterPro; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000515152};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1393
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5028324793"
FT   DOMAIN          29..222
FT                   /note="Thrombospondin-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00210"
FT   REGION          226..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..871
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          885..990
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1047..1217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..344
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..364
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..403
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..434
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..469
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..580
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..609
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..668
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..682
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..775
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..798
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        815..829
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        885..898
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        949..958
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..987
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1071..1089
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1118..1155
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1393 AA;  143618 MW;  728248C084D3DA3A CRC64;
     MLHLLRFVLK LSVCLVLIES TSRAQAAVDL TLQQIVEDPE SSSVERSVDP DGNPAFIFSK
     KSGVSRLAYG LLDSPFHRNF ALLFRLMAAN DTGMLFALTD KSQMRIQLGV KLTRGKLTGR
     QVAVYYSDSK GKTYGKARFA PVAYFPLPTE NHVWTRFAIS FSANKISFFH NCNREPMVGT
     FSRSNAPQLV EAGAAIMVGQ GGHQDGDKFE GQISQLTISG DPAAAERQCY TSDDEDEDDA
     SGSGSGDGID TDTDDGITTR PPKQKTQDVQ LLPEPPVSRT ASKGSLDTGR EETGPKGDSG
     FDTEGSGDTS EQEAPREKGG KVVGSPGMKG DTGPPGPPGP PGPQGPLTEV MDAGDGKVVH
     KVEGRQGPPG PRGPSGQPGP AGRDGQTGEK GDQGVEGAGG PHGFPGTPGN TGMKGQKGEH
     GVGQPGPPGL PGPPGNGETT FVDVEGSGGK MPVRRGPPGL PGPPGPPGPA GSGEDSNGSG
     ASGPNGKPGR PGPSGPMGKA GLPGPPGPRG EKGDCGTLGL PGSGGDTQDG FSVTSFFDNW
     LPYFSSTAAP QGKLGNGGLP GSPGPMGPSG PPGLPGPPGP AGKVTIEQNG TEVTLVEGPP
     GPPGSPGPKG PQGIPGLPGK AGFPGIAGQK GSEGPRGRDG FPGMDGFPGR PGDKGERGLR
     GERGEAGKDG GPPGPPGLPG PPGEIVFPNV GDHEGVVGIA GPPGQPGLAG RAGFPGPMGP
     KGDRGERGQS GVPTKGQKGE PGVILAADGS RLYPGLTSQP GEPGPTGPQG PPGIPGYPGQ
     KGEFGMPGRP GRPGLNGLKG ERGDSVGGHG GYPFPGLPGP PGPPGPPGPA GAVLSLDSFS
     KNGERSRHHP VLKGDKGDQG APGIPGFSGG TGGFDFNAYK NELKGERGDT GMKGEKGEAV
     GGGYYDQRYG GIAGPPGPPG PQGPRGDSVR GPQGPAGPQG QPGYGRPGNP GPPGPPGPQG
     SNLPGAHRSS HTVNVPGPPG PPGPPGVPGL ASGVMVLRTY DSMASISRQQ PEGTLVYITD
     NTDLYIRVRE GCRKVQLGEY TPFPREENNV AAVNPPPVVQ YPPDHTGPDS GASSSSERAP
     PQSEGQSESL EIIPQSGYPH HPASPPRHPS NPSYPFNPAY PPQPGYPPQS GYPPQPGYPP
     QPGYPPQPGY PPQPGYPKYT VTSHGTYPQQ PPPADPRYSP SQPEGRYPDH RYPNGRLPSS
     THRRPSDPQP PASTHEHRAG PALHLIAMNH PQEGNMRGIR GADHECFTQA QAIGMKGTFR
     AFLSSRLQDL YSIVRRSDRE RIPIVNLKDE ELFSSWESIF SESEGKIRAN VTIFSFDGRD
     VLTDDAWPEK MMWHGSSTRG QRVTDSYCET WREANHALTG MASSLQDGRL LQQTQRSCTN
     SYVLLCIENS SIA
//
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